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12 ungesichtete Fragmente: Plagiat

[1.] Ntx/Fragment 008 18 - Diskussion
Bearbeitet: 20. October 2014, 15:23 (Graf Isolan)
Erstellt: 18. October 2014, 22:39 Graf Isolan
Fragment, Kawai und Akari 2006, KomplettPlagiat, Ntx, SMWFragment, Schutzlevel, ZuSichten

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Quelle: Kawai und Akari 2006
Seite(n): 816, Zeilen: 31-52
To date, 10 members of Toll-like receptors (TLRs) have been identified in human, and 13 in mice, and a series of genetic studies have revealed their respective ligands (Fig. 4) (Takeda and Akira 2005a). For example, LPS of Gram-negative bacteria is recognized by TLR4. TLR2, in concert with TLR1 or TLR6, recognizes various bacterial components, including peptidoglycan, lipopeptide and lipoprotein of Gram-positive bacteria and mycoplasma lipopeptide. In particular, TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively. TLR3 recognizes double-stranded RNA (dsRNA) that is produced from many viruses during replication. TLR5 recognizes bacterial flagellin. Mouse TLR11 recognizes yet unknown components of uropathogenic bacteria and a profilin-like molecule of the protozoan parasite Toxoplasma gondii. TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, single-stranded RNA (ssRNA) derived from human immunodeficiency virus type I (HIV-1), vesicular stomatitis virus (VSV) and influenza virus, and certain siRNAs. While mouse TLR8, which shows the highest homology to TLR7, is thought to be nonfunctional, human TLR8 mediates the recognition of imidazoquinolines and ssRNA.
To date, 10 members of Toll-like receptors (TLRs) have been identified in human, and 13 in mice, and a series of genetic studies have revealed their respective ligands (Figure 1).7 For example, LPS of Gram-negative bacteria is recognized by TLR4 (hToll).5,6 TLR2, in concert with TLR1 or TLR6, recognizes various bacterial components, including peptidoglycan, lipopeptide and lipoprotein of Gram-positive bacteria and mycoplasma lipopeptide.8–12 In particular, TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively. TLR3 recognizes double-stranded RNA (dsRNA) that is produced from many viruses during replication.13 TLR5 recognizes bacterial flagellin.14 Mouse TLR11 recognizes yet unknown components of uropathogenic bacteria, and a profilin-like molecule of the protozoan parasite Toxoplasma gondii.15,16 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, single-stranded RNA (ssRNA) derived from human immunodeficiency virus type I (HIV-1), vesicular stomatitis virus (VSV) and influenza virus, and certain siRNAs.17–23 While mouse TLR8, which shows the highest homology to TLR7, is thought to be nonfunctional, human TLR8 mediates the recognition of imidazoquinolines and ssRNA.19–21

5. Poltorak A, He X, Smirnova I, Liu MY, Van Huffel C, Du X, Birdwell D, Alejos E, Silva M, Galanos C, Freudenberg M, Ricciardi-Castagnoli P, Layton B and Beutler B (1998) Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282: 2085–2088

6. Hoshino K, Takeuchi O, Kawai T, Sanjo H, Ogawa T, Takeda Y, Takeda K and Akira S (1999) Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J. Immunol. 162: 3749–3752

7. Takeda K and Akira S (2005) Toll-like receptors in innate immunity. Int. Immunol. 17: 1–14

8. Takeuchi O, Hoshino K, Kawai T, Sanjo H, Takada H, Ogawa T, Takeda K and Akira S (1999) Differential roles of TLR2 and TLR4 in recognition of gramnegative and gram-positive bacterial cell wall components. Immunity 11: 443–451

9. Takeuchi O, Kaufmann A, Grote K, Kawai T, Hoshino K, Morr M, Muhlradt PF and Akira S (2000) Preferentially the R-stereoisomer of the mycoplasmal lipopeptide macrophage-activating lipopeptide-2 activates immune cells through a toll-like receptor 2- and MyD88-dependent signaling pathway. J. Immunol. 164: 554–557

10. Takeuchi O, Sato S, Horiuchi T, Hoshino K, Takeda K, Dong Z, Modlin RL and Akira S (2002) Role of Toll-like receptor 1 in mediating immune response to microbial lipoproteins. J. Immunol. 169: 10–14

11. Takeuchi O, Kawai T, Muhlradt PF, Morr M, Radolf JD, Zychlinsky A, Takeda K and Akira S (2001) Discrimination of bacterial lipoproteins by Toll-like receptor 6. Int. Immunol. 13: 933–940

12. Ozinsky A, Underhill DM, Fontenot JD, Hajjar AM, Smith KD, Wilson CB, Schroeder L and Aderem A (2000) The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between toll-like receptors. Proc. Natl. Acad. Sci. USA 97: 13766–13771

13. Alexopoulou L, Holt AC, Medzhitov R and Flavell RA (2001) Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 413: 732–738

14. Hayashi F, Smith KD, Ozinsky A, Hawn TR, Yi EC, Goodlett DR, Eng JK, Akira S, Underhill DM and Aderem A (2001) The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5. Nature 410: 1099–1103

15. Zhang D, Zhang G, Hayden MS, Greenblatt MB, Bussey C, Flavell RA and Ghosh S (2004) A toll-like receptor that prevents infection by uropathogenic bacteria. Science 303: 1522–1526

16. Yarovinsky F, Zhang D, Andersen JF, Bannenberg GL, Serhan CN, Hayden MS, Hieny S, Sutterwala FS, Flavell RA, Ghosh S and Sher A (2005) TLR11 activation of dendritic cells by a protozoan profilin-like protein. Science 308: 1626–1629

17. Hemmi H, Kaisho T, Takeuchi O, Sato S, Sanjo H, Hoshino K, Horiuchi T, Tomizawa H, Takeda K and Akira S (2002) Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway. Nat. Immunol. 3: 196–200

18. Diebold SS, Kaisho T, Hemmi H, Akira S and Reis e Sousa C (2004) Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science 303: 1529–1531

19. Heil F, Hemmi H, Hochrein H, Ampenberger F, Kirschning C, Akira S, Lipford G, Wagner H and Bauer S (2004) Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8. Science 303: 1526–1529

20. Heil F, Ahmad-Nejad P, Hemmi H, Hochrein H, Ampenberger F, Gellert T, Dietrich H, Lipford G, Takeda K, Akira S, Wagner H and Bauer S (2003) The Toll-like receptor 7 (TLR7)-specific stimulus loxoribine uncovers a strong relationship within the TLR7 8 and 9 subfamily. Eur. J. Immunol. 33: 2987–2997

21. Jurk M, Heil F, Vollmer J, Schetter C, Krieg AM, Wagner H, Lipford G and Bauer S (2002) Human TLR7 or TLR8 independently confer responsiveness to the antiviral compound R-848. Nat. Immunol. 3: 499

Anmerkungen

Ohne Hinweis auf eine Übernahme. Für die angegebene Referenz existiert kein Eintrag im Literaturverzeichnis.

Sichter
(Graf Isolan)

[2.] Ntx/Fragment 013 16 - Diskussion
Bearbeitet: 20. October 2014, 15:24 (Graf Isolan)
Erstellt: 19. October 2014, 19:59 Graf Isolan
Castera et al 2009, Fragment, KomplettPlagiat, Ntx, SMWFragment, Schutzlevel, ZuSichten

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Mitochondria initiate apoptosis through mitochondrial outer membrane permeabilization and the release of apoptogenic factors (e.g cytochrome c, AIF- apoptosis inducing factor) from the mitochondrial intermembrane space, leading to cell death through caspase-dependent and –independent pathways (Green and Reed 1998a; Mohamad et al 2005).

[...] Signaling cascades can also affect the inner mitochondrial membrane permeability in apoptosis and necrosis. As a consequence, cells also exhibit a loss of electrical potential across the inner membrane which is quantifiable by means of potentiometric dyes (Marchetti et al 1996).

[...] Mitochondrial dysfunction, characterized by marked reduction in mitochondrial membrane potential (Δψm), is an early step of ongoing DC death that can be triggered by many cytotoxic stimuli (McLellan et al 2000; Nencioni et al 2006b; Vassiliou et al 2004a).


Green,D.R., Reed,J.C., 1998a. Mitochondria and apoptosis. Science 281, 1309-1312.

Marchetti,P., Castedo,M., Susin,S.A., Zamzami,N., Hirsch,T., Macho,A., Haeffner,A., Hirsch,F., Geuskens,M., Kroemer,G., 1996. Mitochondrial permeability transition is a central coordinating event of apoptosis. J. Exp. Med. 184, 1155-1160.

McLellan,A.D., Terbeck,G., Mengling,T., Starling,G.C., Kiener,P.A., Gold,R., Brocker,E.B., Leverkus,M., Kampgen,E., 2000. Differential susceptibility to CD95 (Apo-1/Fas) and MHC class II-induced apoptosis during murine dendritic cell development. Cell Death. Differ. 7, 933-938.

Mohamad,N., Gutierrez,A., Nunez,M., Cocca,C., Martin,G., Cricco,G., Medina,V., Rivera,E., Bergoc,R., 2005. Mitochondrial apoptotic pathways. Biocell 29, 149-161.

Nencioni,A., Garuti,A., Schwarzenberg,K., Cirmena,G., Dal Bello,G., Rocco,I., Barbieri,E. Brossart,P., Patrone,F., Ballestrero,A., 2006a. Proteasome inhibitor-induced apoptosis in human monocyte-derived dendritic cells. Eur. J. Immunol. 36, 681-689.

Vassiliou,E., Sharma,V., Jing,H., Sheibanie,F., Ganea,D., 2004a. Prostaglandin E2 promotes the survival of bone marrow-derived dendritic cells. J. Immunol. 173, 6955-6964.

Mitochondria initiate apoptosis through mitochondrial outer membrane permeabilization and the release of apoptogenic factors (e.g. cytochrome c, AIF or Smac/Diablo) from the mitochondrial intermembrane space, leading to cell death through caspase-dependent and -independent pathways. Signalling cascades can also affect the inner mitochondrial membrane permeability in apoptosis and necrosis. As a consequence, cells also exhibit a loss of electrical potential across the inner membrane which is quantifiable by means of potentiometric dyes, a measure that precedes signs of nuclear apoptosis and cell death [6]. Mitochondrial dysfunction, characterized by marked reduction in mitochondrial membrane potential (Δψm), is an early step of ongoing DC death that can be triggered by many cytotoxic stimuli [7–13].

6. Marchetti P, Castedo M, Susin SA, et al. Mitochondrial permeability transition is a central coordinating event of apoptosis. J Exp Med. 1996; 184: 1155–60.

7. McLellan AD, Terbeck G, Mengling T, et al. Differential susceptibility to CD95 (Apo-1/Fas) and MHC class II-induced apoptosis during murine dendritic cell development. Cell Death Differ. 2000; 7: 933–8.

8. Jin H, Xiao C, Zhao G, Du X, et al. Induction of immature dendritic cell apoptosis by foot and mouth disease virus is an integrin receptor mediated event before viral infection. J Cell Biochem. 2007; 102: 980–91.

9. Nencioni A, Garuti A, Schwarzenberg K, et al. Proteasome inhibitor-induced apoptosis in human monocyte-derived dendritic cells. Eur J Immunol. 2006; 36: 681–9.

10. Vassiliou E, Sharma V, Jing H, et al. Prostaglandin E2 promotes the survival of bone marrow-derived dendritic cells. J Immunol. 2004; 173: 6955–64.

11. Sanchez-Sanchez N, Riol-Blanco L, de la Rosa G, et al. Chemokine receptor CCR7 induces intracellular signaling that inhibits apoptosis of mature dendritic cells. Blood. 2004; 104: 619–25.

12. Nicolo C, Tomassini B, Rippo MR, Testi R. UVB-induced apoptosis of human dendritic cells: contribution by caspase-dependent and caspase-independent pathways. Blood. 2001; 97: 1803–8.

13. Leverkus M, McLellan AD, Heldmann M, et al. MHC class II-mediated apoptosis in dendritic cells: a role for membrane-associated and mitochondrial signaling pathways. Int Immunol. 2003; 15: 993–1006. 2004; 104: 619–25.

Anmerkungen

Kein Hinweis auf die eigentliche Quelle. Art und Umfang der Übernahme bleiben ungekennzeichnet.

Sichter
(Graf Isolan)

[3.] Ntx/Fragment 014 01 - Diskussion
Bearbeitet: 21. October 2014, 20:12 (Graf Isolan)
Erstellt: 19. October 2014, 20:57 Graf Isolan
Castera et al 2009, Fragment, KomplettPlagiat, Ntx, SMWFragment, Schutzlevel, ZuSichten

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[Compelling evidence] indicates that mitochondria-related proteins of the Bcl-2 family are crucial DC death sensors (Nencioni et al 2006a; Nicolo et al 2001; Vassiliou et al 2004b), substantiating the importance of mitochondria in DC apoptosis.

'1.10.2. Extrinsic apoptosis pathway

It is mediated by death receptors, such as the receptors for Fas and tumor necrosis factor (TNF)- related apoptosis-inducing ligand (TRAIL), and caspase-8, i.e. the major initiator caspase in this pathway. Several death receptors, including Fas, are expressed in DCs. However, DCs are known to be resistant to Fas-induced cell death through the constitutive expression of FLICE–like inhibitory protein (FLIP), a strong inhibitor of apoptosis initiated by death receptors (Willems et al 2000)


Nencioni,A., Garuti,A., Schwarzenberg,K., Cirmena,G., Dal Bello,G., Rocco,I., Barbieri,E., Brossart,P., Patrone,F., Ballestrero,A., 2006a. Proteasome inhibitor-induced apoptosis in human monocyte-derived dendritic cells. Eur. J. Immunol. 36, 681-689.

Nicolo,C., Tomassini,B., Rippo,M.R., Testi,R., 2001. UVB-induced apoptosis of human dendritic cells: contribution by caspase-dependent and caspase-independent pathways. Blood 97, 1803-1808.

Willems,F., Amraoui,Z., Vanderheyde,N., Verhasselt,V., Aksoy,E., Scaffidi,C., Peter,M.E., Krammer,P.H., Goldman,M., 2000. Expression of c-FLIP(L) and resistance to CD95-mediated apoptosis of monocyte-derived dendritic cells: inhibition by bisindolylmaleimide. Blood 95, 3478-3482.

The extrinsic apoptosis pathway is mediated by death receptors, such as the receptors for Fas and tumour necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL), and caspase-8, i.e. the major initiator caspase in this pathway. Several death receptors, including Fas, are expressed in monocyte-derived DCs. However, DCs are known to be resistant to Fas-induced cell death through the constitutive expression of FLICE (caspase-8)-like inhibitory protein (FLIP), a strong inhibitor of apoptosis initiated by death receptors [5].

[...]

[...] Compelling evidence indicates that mitochondria-related proteins of the Bcl-2 family are crucial DC death sensors [9, 12, 14–16], substantiating the importance of mitochondria in DC apoptosis.


5. Willems F, Amraoui Z, Vanderheyde N, et al. Expression of c-FLIP(L) and resistance to CD95-mediated apoptosis of monocyte-derived dendritic cells: inhibition by bisindolylmaleimide. Blood. 2000; 95: 3478–82.

9. Nencioni A, Garuti A, Schwarzenberg K, et al. Proteasome inhibitor-induced apoptosis in human monocyte-derived dendritic cells. Eur J Immunol. 2006; 36: 681–9.

12. Nicolo C, Tomassini B, Rippo MR, Testi R. UVB-induced apoptosis of human dendritic cells: contribution by caspase-dependent and caspase-independent pathways. Blood. 2001; 97: 1803–8.

14. Kriehuber E, Bauer W, Charbonnier AS, et al. Balance between NF-{kappa}B and JNK(AP-1 activity controls dendritic cell life and death. Blood. 2005; 106: 175–83.

15. Hou WS, Van Parijs L. A Bcl-2-dependent molecular timer regulates the lifespan and immunogenicity of dendritic cells. Nat Immunol. 2004; 5: 583–9.

16. Kim TW, Lee JH, He L, et al. Modification of professional antigen-presenting cells with small interfering RNA in vivo to enhance cancer vaccine potency. Cancer Res. 2005; 65: 309–16.

Anmerkungen

Eine Referenz für "Vassiliou et al 2004b" findet sich nicht im Literaturverzeichnis von Ntx. Kein Hinweis auf eine Übernahme.

Sichter
(Graf Isolan)

[4.] Ntx/Fragment 016 17 - Diskussion
Bearbeitet: 20. October 2014, 13:46 (Graf Isolan)
Erstellt: 20. October 2014, 10:36 Graf Isolan
Feinstein-Rotkopf und Arama 2009, Fragment, Ntx, SMWFragment, Schutzlevel, Verschleierung, ZuSichten

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Seite(n): 980-981, Zeilen: 980:re.Sp. 16-21.27-31 - 981:li.Sp. 1-3.5-11
1.10.6. Caspase activity

Caspases, a unique family of cysteine-dependent aspartate specific proteases, play a pivotal role in cell death. The mammalian genome encodes fourteen distinct caspases, seven of which were shown to function in apoptosis (Chowdhury et al 2008).

Initiator caspases are activated through dimerization facilitated at multi-protein complexes. Activation of caspase-9, the initiator caspase of the intrinsic pathway, while the apical caspase of the extrinsic apoptotic pathway caspase-8 is activated within the death-inducing signaling complex (DISC) (Ashkenazi and Dixit 1998; Boatright and Salvesen 2003b). On the other hand, activation of effector caspases, such as caspase-3 and -7 occurs upon their cleavage at specific internal aspartic acid residues by initiator caspases (Boatright and Salvesen 2003a). Downstream of this activational cascade, caspases cleave a variety of regulatory and structural proteins and important enzymes, ultimately leading to cell death (Gradzka 2006; Pop and Salvesen 2009).


Ashkenazi,A., Dixit,V.M., 1998. Death receptors: signaling and modulation. Science 281, 1305-1308.

Boatright,K.M., Salvesen,G.S., 2003a. Mechanisms of caspase activation. Curr. Opin. Cell Biol. 15, 725-731.

Chowdhury,I., Tharakan,B., Bhat,G.K., 2008. Caspases - an update. Comp Biochem. Physiol Biochem. Mol. Biol. 151, 10-27.

Gradzka,I., 2006. [Mechanisms and regulation of the programmed cell death]. Postepy Biochem. 52, 157-165.

Pop,C., Salvesen,G.S., 2009. Human caspases: Activation, specificity and regulation. J. Biol. Chem.

[Seite 980]

Introduction

[...] A key feature of apoptosis is the activation of a unique family of cysteine-dependent aspartate specific proteases called caspases. The mammalian genome encodes fourteen distinct caspases, seven of which were shown to function in apoptosis and will henceforth be termed apoptotic caspases or simply caspases [16, 17].

[...] Initiator caspases are activated through dimerization facilitated at multi-protein complexes. Activation of caspase-9, the initiator caspase of the intrinsic pathway, involves its recruitment to the apoptosome by Apaf-1-Cyt c complex,

[Seite 981]

while the apical caspase of the extrinsic apoptotic pathway caspase-8 is activated within the death-inducing signaling complex (DISC) [25–29]. [...] On the other hand, activation of effector caspases, such as caspase-3 and -7 occurs upon their cleavage at specific internal aspartic acid residues by initiator caspases [28, 29]. Downstream of this activational cascade, caspases cleave a variety of regulatory and structural proteins and important enzymes, ultimately leading to cell death.


16. Petrilli V, Dostert C, Muruve DA, Tschopp J (2007) The inflammasome: a danger sensing complex triggering innate immunity. Curr Opin Immunol 19:615–622. doi:10.1016/j.coi.2007.09.002

17. Chowdhury I, Tharakan B, Bhat GK (2008) Caspases — an update. Comp Biochem Physiol B Biochem Mol Biol 151:10–27. doi:10.1016/j.cbpb.2008.05.010

25. Zou H, Henzel WJ, Liu X, Lutschg A, Wang X (1997) Apaf-1, a human protein homologous to C elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90:405–413. doi:10.1016/S0092-8674(00)80501-2

26. Ashkenazi A, Dixit VM (1998) Death receptors: signaling and modulation. Science 281:1305–1308. doi:10.1126/science.281.5381.1305

27. Rodriguez J, Lazebnik Y (1999) Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev 13:3179–3184. doi:10.1101/gad.13.24.3179

28. Boatright KM, Salvesen GS (2003) Mechanisms of caspase activation. Curr Opin Cell Biol 15:725–731. doi:10.1016/j.ceb.2003.10.009

29. Riedl SJ, Shi Y (2004) Molecular mechanisms of caspase regulation during apoptosis. Nat Rev Mol Cell Biol 5:897–907. doi:10.1038/nrm1496

Anmerkungen

Ohne Hinweis auf eine Übernahme.

Sichter
(Graf Isolan)

[5.] Ntx/Fragment 001 22 - Diskussion
Bearbeitet: 27. November 2014, 20:31 (Graf Isolan)
Erstellt: 21. October 2014, 05:19 SleepyHollow02
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• Natural killer cells (NK), Natural killer T cells (NK T) and T cell receptor γδ (TCR-γδ) lymphocytes constitute particular populations of lymphocytes which play important roles in innate immunity and share similar functions upon activation, such as expansion, secretion of soluble factors (cytokines, chemokines) and cytolytic activity (Hamerman et al 2005; Lauwerys et al 2000; Vivier 2006).

Hamerman,J.A., Ogasawara,K., Lanier,L.L., 2005. NK cells in innate immunity. Curr. Opin. Immunol. 17, 29-35.

Lauwerys,B.R., Garot,N., Renauld,J.C., Houssiau,F.A., 2000. Cytokine production and killer activity of NK/T-NK cells derived with IL-2, IL-15, or the combination of IL-12 and IL-18. J. Immunol. 165, 1847-1853.

Vivier,E., 2006. What is natural in natural killer cells? Immunol. Lett. 107, 1-7.

Natural killer, NK T and TCR-γδ lymphocytes constitute particular populations of lymphocytes which play important roles in innate immunity and share similar functions upon activation, such as expansion, secretion of soluble factors (cytokines, chemokines) and cytolytic activity [19–22].

19 Hamerman JA, Ogasawara K, Lanier LL. NK cells in innate immunity. Curr Opin Immunol 2005; 17:29–35.

20 Hayday AC. [Gamma][delta] cells: a right time and a right place for a conserved third way of protection. Annu Rev Immunol 2000;18:975–1026.

21 Lauwerys BR, Garot N, Renauld JC, Houssiau FA. Cytokine production and killer activity of NK/T–NK cells derived with IL-2, IL-15, or the combination of IL-12 and IL-18. J Immunol 2000;165:1847–53.

22 Vivier E.What is natural in natural killer cells? Immunol Lett 2006; 107:1–7.

Anmerkungen
Sichter
(SleepyHollow02)

[6.] Ntx/Fragment 007 01 - Diskussion
Bearbeitet: 21. October 2014, 05:36 (SleepyHollow02)
Erstellt: 21. October 2014, 05:33 SleepyHollow02
Fragment, Ntx, Reschner et al 2008, SMWFragment, Schutzlevel, Verschleierung, ZuSichten

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The cross-talk between innate cells and DCs which leads to innate lymphocyte activation and DC maturation was found to be multi-directional, involving not only cell–cell contacts but also soluble factors. The final outcome of these cellular interactions may have a dramatic impact on the quality and strength of the down-stream immune responses. In addition to their role in induction of adaptive immune responses, DCs also activate natural killer (NK) cells (Fernandez et al 1999) and can produce large amounts of interferon upon encounter with viral pathogens (Kadowaki et al 2000), thus, providing a link between the adaptive and innate immune system. More recently, DC activating ability was extended to other cell types such as NK T or TCR-γδ cells (Takahashi et al 2002). Moreover, certain DC subsets share common developmental pathways with NK cells, suggesting that these cells could influence each other during differentiation (Marquez et al 1998).

Fernandez,N.C., Lozier,A., Flament,C., Ricciardi-Castagnoli,P., Bellet,D., Suter,M., Perricaudet,M., Tursz,T., Maraskovsky,E., Zitvogel,L., 1999. Dendritic cells directly trigger NK cell functions: cross-talk relevant in innate anti-tumor immune responses in vivo. Nat. Med. 5, 405-411.

Kadowaki,N., Antonenko,S., Lau,J.Y., Liu,Y.J., 2000. Natural interferon alpha/betaproducing cells link innate and adaptive immunity. J. Exp. Med. 192, 219-226.

Takahashi,T., Chiba,S., Nieda,M., Azuma,T., Ishihara,S., Shibata,Y., Juji,T., Hirai,H., 2002. Cutting edge: analysis of human V alpha 24+CD8+ NK T cells activated by alphagalactosylceramide-pulsed monocyte-derived dendritic cells. J. Immunol. 168, 3140- 3144.

Marquez,C., Trigueros,C., Franco,J.M., Ramiro,A.R., Carrasco,Y.R., Lopez-Botet,M., Toribio,M.L., 1998. Identification of a common developmental pathway for thymic natural killer cells and dendritic cells. Blood 91, 2760-2771.

The cross-talk between innate cells and DC which leads to innate lymphocyte activation and DC maturation was found to be multi-directional, involving not only cell–cell contacts but also soluble factors. The final outcome of these cellular interactions may have a dramatic impact on the quality and strength of the down-stream immune responses, mainly in the context of early responses to tumour cells and infectious agents.

In addition to their role in induction of adaptive immune responses, DC also activate natural killer (NK) cells [13]. More recently, this DC activation was extended to other cell types such as NK T or T cell receptor (TCR)-gd cells [14,15]. Moreover, certain DC subsets share common developmental pathways with NK cells, suggesting that these cells could influence each other during differentiation [16–18].


13 Fernandez NC, Lozier A, Flament C et al. Dendritic cells directly trigger NK cell functions: cross-talk relevant in innate anti-tumor immune responses in vivo. Nat Med 1999; 5:405–11.

16 Blom B, Spits H. Development of human lymphoid cells. Annu Rev Immunol 2006; 24:287–320.

17 Marquez C, Trigueros C, Franco JM et al. Identification of a common developmental pathway for thymic natural killer cells and dendritic cells. Blood 1998; 91:2760–71.

18 Perez SA, Sotiropoulou PA, Gkika DG et al. A novel myeloid-like NK cell progenitor in human umbilical cord blood. Blood 2003; 101:3444–50.

Anmerkungen
Sichter
(SleepyHollow02)

[7.] Ntx/Fragment 010 12 - Diskussion
Bearbeitet: 21. October 2014, 05:43 (SleepyHollow02)
Erstellt: 21. October 2014, 05:40 SleepyHollow02
Fragment, Ntx, Reschner et al 2008, SMWFragment, Schutzlevel, Verschleierung, ZuSichten

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Table 1: Populations of DCs in mice and humans.

DC subsets Tissue distribution Species Immature phenotype Mature phenotype Bone marrow derived DC Dermis, airways, intestine, thymus, spleen, liver, lymphoid tissue Mouse CD11c+CD8α- CD11b+MHCII+ TLR-1–3+/−TLR-2,4–9+ CD83+ CCR7+ CD80++ CD86++ MHCII++ Human CD1a+ CD14- CD11c++CD11b++ CD1c+ CD209+ MHC-II+ TLR-1, 6+,3,8++ CD40+ Plasmacytoid DC Lymphoid organs, liver, lung, skin Mouse CD11c+/−B220+Ly-6C+CD11b- PDCA+ MHC-II+ TLR-2–9+ Human CD14-CD11c-CD123++ BDCA2+ ILT7+ MHC-II+ TLR-7,9++ CD8α+DC Thymus, spleen, lymph node, liver Mouse CD8α+CD4-CD11c++ CD11b CD205++-TLR-2–4,6,8,9+ Human Not identified Langerhans cells Mucosal epithelia, epidermis Mouse CD8α- CD11c+ CD205++ Ecadherin+ CD207+ E-cadherin +/− Human CD14+/−CD11c+CD1a+ Ecadherin+ CD207+CCR6+ DC, dendritic cells. +/−, low; ++, high.

Table 1. Populations of DC in mice and humans. DC subsets Tissue distribution Species Immature phenotype Mature phenotype Bone marrow derived DC Dermis, airways, intestine, thymus, spleen, liver, lymphoid tissue Mouse CD11c+CD8a- CD11b+MHC-II+ TLR-1–3+/-TLR-2,4–9+ CD83+ CCR7+ CD80++ CD86++ MHC-II++ Human CD1a+ CD14-CD11c++CD11b++ CD1c+ CD209+ MHC-II+ TLR-1, 6+,3,8++ CD40+ Plasmacytoid DC Lymphoid organs, liver, lung, skin Mouse CD11c+/-B220+Ly-6C+CD11b- PDCA+ MHC-II+ TLR-2–9+ Human CD14-CD11c-CD123+ + BDCA2+ ILT7+ MHC-II+ TLR-7,9++ CD8a+DC Thymus, spleen, lymph node, liver Mouse CD8a+CD4-CD11c++ CD11b CD205++ -TLR-2–4,6,8,9+ Human Not identified Langerhans cells Mucosal epithelia, epidermis Mouse CD8a- CD11c+ CD205++ E-cadherin+CD207+ E-cadherin +/- Human CD14+/-CD11c+CD1a+ E-cadherin+CD207+CCR6+ DC, dendritic cells. +/-, low; ++, high.
Anmerkungen
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1.8. The mucosal immune system

Most of our encounters with antigens or infectious agents occur at mucosal surfaces, which include the surface lining the gastrointestinal, respiratory and genitourinary tracts (Delves and Roitt 2000). Since nutrients are usually absorbed orally, they are thus ideally suited to influence the immune response at the “mucosal frontier” of the gastrointestinal tract, representing more than 300 m2. Well known for its nutrition function (digestion of food and the assimilation of the nutrients), the intestinal system is also able to protect us from the pathogenic microbes. It contains more than 100 million neurons, secretes at least 20 neurotransmitters identical to those produced by the brain (serotonin, noradrenalin, dopamine, etc.), produces 70 to 85 % of the immune cells of the organism, lodges 100 000 billion bacteria. All these compounds, present locally, are in relationship to the whole of the organism (Delcenserie et al 2008). Although the immune response of the intestinal mucosa exhibits several features in common with the immune responses produced by other organs, it is characterized by certain distinctive [properties.]

2. The mucosal immune system

Most of our encounters with antigens or infectious agents occur at mucosal surfaces, which include the surface lining the gastrointestinal, respiratory and genitourinary tracts (Delves and Roitt, 2000). Since probiotics are usually absorbed orally, they are thus ideally suited to influence the immune response at the “mucosal frontier” of the gastrointestinal tract, representing more than 300 m2.

Well known for its nutrition function (digestion of food and the assimilation of the nutrients), the intestinal system is also able to protect us from the pathogenic microbes. It contains more than 100 million neurons, secretes at least 20 neurotransmitters identical to those produced by the brain (serotonin, noradrenalin, dopamine...), produces 70 to 85 % of the immune cells of the organism, lodges 100 000 billion bacteria. All these compounds, present locally, are in relationship to the whole of the organism. Although the immune response of the intestinal mucosa exhibits several features in common with the immune responses produced by other organs, it is characterized by certain distinctive properties.

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The immune properties of the digestive mucosa are provided by the GALT (Gut-associated lymphoid tissue). The GALT is composed of lymphoid aggregates, including the Peyer’s patches (located mainly in the small intestinal distal ileum), where induction of immune responses occurs, and mesenteric lymphoid nodes. In addition, there are large amounts of immune-competent cells in the lamina propria and the mucosal epithelium (Delcenserie et al 2008).

The intestine also protects us from pathogens because its epithelium is covered by mucus and avoids any direct contact with the microorganisms. The intestinal immune system must encounter all antigens in order to determine which ones require an immune response and which ones can be safely tolerated (Delcenserie et al 2008).

The intestinal immune system is the subject of complex regulation processes allowing the elimination of pathogenic microorganisms, while maintaining a tolerance towards food antigens and endogenous flora. Butyrate as well as other products resulting from colic fermentation, could take part in this regulation (Marteau et al 2004).

1.9. Mucosal dendritic cells

[...] It has been shown that DCs, using their dendrites, act as guard cells in the intestinal lumen without disturbing the integrity of their tight surface junctions (Niess 2008).


Delcenserie,V., Martel,D., Lamoureux,M., Amiot,J., Boutin,Y., Roy,D., 2008. Immunomodulatory effects of probiotics in the intestinal tract. Curr. Issues Mol. Biol. 10, 37-54.

Marteau,P., Seksik,P., Lepage,P., Dore,J., 2004. Cellular and physiological effects of probiotics and prebiotics. Mini. Rev. Med. Chem. 4, 889-896.

Niess,J.H., 2008. Role of mucosal dendritic cells in inflammatory bowel disease. World J. Gastroenterol. 14, 5138-5148.

The immune properties of the digestive mucosa are provided by the GALT (Gut-associated lymphoid tissue). The GALT is composed of lymphoid aggregates, including the Peyer’s patches (located mainly in the small intestinal distal ileum), where induction of immune responses occurs, and mesenteric lymphoid nodes. In addition, there are large amounts of immune-competent cells in the lamina propria and the mucosal epithelium. The intestine also protects us from pathogens because its epithelium is covered by mucus and avoids any direct contact with the micro-organisms. The intestinal immune system must encounter all antigens in order to determine which ones require an immune response and which ones can be safely tolerated.

[...] Finally, it has been shown that DCs, using their dendrites, also act as guard cells in the intestinal lumen without disturbing the integrity of their tight surface junctions. [...] The intestinal immune system is the subject of complex regulation processes allowing the elimination of pathogenic micro-organisms, while maintaining a tolerance towards food antigens and endogenous flora. Butyrate as well as other products resulting from colic fermentation, could take part in this regulation.

Anmerkungen

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[Defects in this regulation are supposed to lead to the several forms of inflammatory disease such as: Crohn's disease (CD) and ulcerative colitis (UC) (MacDonald and Monteleone 2005)] and hemorrhagic rectocolitis (HRC), a deregulation of the intestinal immune system would lead to an inadequate response against one or more endoluminal antigens. An imbalance between Th1 (IL-2, IFNγ, T N F α ) and Th2 responses (IL-4, IL-5, IL-10) was described in human and also in animal models (Zeitz et al 1990). This led to a chronic inflammatory answer characterized by the production of pro-inflammatory cytokines (IL-1, IL-6, TNFα). Thus, the cytokine profile plays an important role in the maintenance of intestinal immune homeostasis (Niess 2008).

MacDonald,T.T., Monteleone,G., 2005. Immunity, inflammation, and allergy in the gut. Science 307, 1920-1925.

Niess,J.H., 2008. Role of mucosal dendritic cells in inflammatory bowel disease. World J. Gastroenterol. 14, 5138-5148.

In chronic intestinal inflammatory diseases (CIID) such as Crohn’s disease (Macdonald and Monteleone, 2005 ; MacDonald et al., 2000) and hemorrhagic rectocolitis (HRC), a deregulation of the intestinal immune system would lead to an inadequate response against one or more endoluminal antigens. An imbalance between Th1 (IL-2, IFNγ, T N F α ) and Th2 responses (IL-4, IL-5, IL-10) was described in human and also in animal models. This led to a chronic inflammatory answer characterized by the production of pro-inflammatory cytokines (IL-1, IL-6, TNFα).

[...] Thus, the cytokine profile plays an important role in the maintenance of intestinal immune homeostasis.


Macdonald, T.T., and Monteleone, G. (2005). Immunity, inflammation, and allergy in the gut. Science 307, 1920-1925.

Anmerkungen

Niess (2008) wäre die Quellenangabe für weite Teile des Materials gewesen, das auf der voran gegangenen Seite präsentiert wurde.

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1.9. Mucosal dendritic cells

Mucosal DCs are assumed to play key roles in regulating immune responses in the antigen-rich gastrointestinal environment. [...] Mucosal DCs are a heterogeneous population that can either initiate (innate and adaptive) immune responses, or control intestinal inflammation and maintain tolerance (Nagler-Anderson 2001; Steinman and Nussenzweig 2002b).

The intestinal innate and adaptive immune system has evolved in response to potent stimuli derived from constituents of the commensal microflora. In most cases these local immune responses achieve tolerance to the intestinal microflora and food antigens. Tolerance to intestinal self antigens, oral antigens and the commensal flora is achieved by interactions of DCs with regulatory and effector T cells. Local T cell immunity is an important compartment of the specific intestinal immune system. T cell reactivity is programmed during the initial stage of its activation by DCs (Medzhitov and Janeway, Jr. 1999).

DCs reside in mucosal tissues or recirculate in the blood and lymphoid tissues (Iwasaki 2007). The lamina propria of the small and large intestine are effector sites of mucosal tissues. The local microenvironment influences the phenotype of DCs, and are characterized by a remarkable plasticity between DCs (Kelsall and Rescigno 2004). In the lamina propria of the small and large intestine, DCs are ideally situated to survey the constituents of the commensal microflora and monitor food antigens (Bjorck 2001).

Defects in this regulation are supposed to lead to the several forms of inflammatory disease such as: Crohn's disease (CD) and ulcerative colitis (UC) (MacDonald and Monteleone 2005) [and hemorrhagic rectocolitis (HRC), a deregulation of the intestinal immune system would lead to an inadequate response against one or more endoluminal antigens.]


Bjorck,P., 2001. Isolation and characterization of plasmacytoid dendritic cells from Flt3 ligand and granulocyte-macrophage colony-stimulating factor-treated mice. Blood 98, 3520-3526.

Iwasaki,A., 2007. Mucosal dendritic cells. Annu. Rev. Immunol. 25, 381-418.

Kelsall,B.L., Rescigno,M., 2004. Mucosal dendritic cells in immunity and inflammation. Nat. Immunol. 5, 1091-1095.

MacDonald,T.T., Monteleone,G., 2005. Immunity, inflammation, and allergy in the gut. Science 307, 1920-1925.

Medzhitov,R., Janeway,C.A., Jr., 1999. Innate immune induction of the adaptive immune response. Cold Spring Harb. Symp. Quant. Biol. 64, 429-435.

Nagler-Anderson,C., 2001. Man the barrier! Strategic defences in the intestinal mucosa. Nat. Rev. Immunol. 1, 59-67.

[Seite 5138]

Abstract

[...] Mucosal dendritic cells (DCs) are assumed to play key roles in regulating immune responses in the antigen-rich gastrointestinal environment. Mucosal DCs are a heterogeneous population that can either initiate (innate and adaptive) immune responses, or control intestinal inflammation and maintain tolerance. Defects in this regulation are supposed to lead to the two major forms of inflammatory bowel disease (IBD), Crohn’s disease (CD) and ulcerative colitis (UC). [...] The local microenvironment influences the phenotype of DCs, a heterogeneous population that can be divided into conventional DCs (CD8α+CD11b-, CD4+CD11b+, CD4-CD11b+)[7,8] and plasmacytoid DCs (B220+CD11clow) (Table 2) and are characterized by a remarkable plasticity between DCs[9]. In the lamina propria of the small and large intestine, DCs are ideally situated to survey the constituents of the commensal microflora and monitor food antigens[10].

[...]

INTRODUCTION

The intestinal innate and adaptive immune system has evolved in response to potent stimuli derived from constituents of the commensal microflora. In most cases these local immune responses achieve tolerance to the intestinal microflora and food antigens. Defects of the tightly regulated mucosal immune responses are assumed to result in inflammatory bowel disease (IBD), such as Crohn’s disease (CD) and ulcerative colitis (UC)[1,2]. Local T cell immunity is an important compartment of the specific intestinal immune system. T cell reactivity is programmed during the initial stage of its activation by dendritic cells (DCs) that can either initiate (innate and adaptive) immune responses, or control intestinal inflammation and maintain tolerance[3-5].DCs reside in mucosal tissues or recirculate in the blood and lymphoid tissues[6]. The lamina propria of the small and large intestine are effector sites of mucosal tissues.

[Seite 5144]

CONCLUSION

[...] Tolerance to intestinal self antigens, oral antigens and the commensal flora is achieved by interactions of DCs with regulatory and effector T cells.


1 Xavier RJ, Podolsky DK. Unravelling the pathogenesis of inflammatory bowel disease. Nature 2007; 448: 427-434

2 Strober W. Immunology. Unraveling gut inflammation. Science 2006; 313: 1052-1054

3 Nagler-Anderson C. Man the barrier! Strategic defences in the intestinal mucosa. Nat Rev Immunol 2001; 1: 59-67

4 Niess JH, Reinecker HC. Dendritic cells in the recognition of intestinal microbiota. Cell Microbiol 2006; 8: 558-564

5 Steinman RM, Nussenzweig MC. Avoiding horror autotoxicus: the importance of dendritic cells in peripheral T cell tolerance. Proc Natl Acad Sci US 2002; 99: 351-358

6 Iwasaki A. Mucosal dendritic cells. Annu Rev Immunol 2007; 25: 381-418

7 Vremec D, Shortman K. Dendritic cell subtypes in mouse lymphoid organs: cross-correlation of surface markers, changes with incubation, and differences among thymus, spleen, and lymph nodes. J Immunol 1997; 159: 565-573

8 Hochrein H, Shortman K, Vremec D, Scott B, Hertzog P, O'Keeffe M. Differential production of IL-12, IFN-alpha, and IFN-gamma by mouse dendritic cell subsets. J Immunol 2001; 166: 5448-5455

9 Kelsall BL, Rescigno M. Mucosal dendritic cells in immunity and inflammation. Nat Immunol 2004; 5: 1091-1095

10 Bjorck P. Isolation and characterization of plasmacytoid dendritic cells from Flt3 ligand and granulocytemacrophage colony-stimulating factor-treated mice. Blood 2001; 98: 3520-3526

Anmerkungen

Im Literaturverzeichnis findet sich keine Referenz für Steinman and Nussenzweig (2002b).

Auf der Folgeseite, wo noch ein Absatz folgt, der nicht aus Niess (2008), sondern aus Delcenserie et al (2008) stammt (vgl. Ntx/Fragment_013_01) wird die Quelle am Ende dieses Absatzes (endlich) genannt.

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[12.] Ntx/Fragment 006 05 - Diskussion
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DCs activate naïve Th cells by: 1) the antigen-specific recognition of peptides in the context of MHC molecules on the DC by TCR; 2) co-stimulatory molecules CD80 and CD86 which bind to CD28 on the T cell (Linsley et al 1990) and direct T-cell differentiation into various subsets such as Th1 and Th2 by secreting polarizing cytokines which bind to their receptors on the T cell (Scott 1993). A given Th-cell subset is characterized by its cytokine-secretion profile which is intimately associated to the effector functions. Th1 cells mediate cellular immunity against intracellular bacteria and viruses by secreting cytokines such as IFN-γ and tumour necrosis factor-α (TNF-α), Th2 cells regulate humoral immunity and immunity against extracellular parasites by producing IL-4, IL-5 and IL-13 (Corthay 2006).

Corthay,A., 2006. A three-cell model for activation of naive T helper cells. Scand. J. Immunol. 64, 93-96.

Linsley,P.S., Clark,E.A., Ledbetter,J.A., 1990. T-cell antigen CD28 mediates adhesion with B cells by interacting with activation antigen B7/BB-1. Proc. Natl. Acad. Sci. U. S. A 87, 5031-5035.

Scott,P., 1993. IL-12: initiation cytokine for cell-mediated immunity. Science 260, 496-497.

Immunology students are usually taught that the activation of naı¨ve Th cells is the result of a two-cell interaction between the Th cell and a dendritic cell (DC), and that three signals are involved (Fig. 1A). Signal one is the antigen-specific recognition of peptides in the context of major histocompatibility complex (MHC) molecules on the DC by the T-cell receptor (TCR) [1, 2]. Signal two is provided by the co-stimulatory molecules CD80 and CD86 which bind to CD28 on the T cell [3, 4]. [...] Signal three, which relies on the binding of a polarizing cytokine to its receptor on the T cell, directs T-cell differentiation into various subsets such as Th1 and Th2 [7]. A given Th-cell subset is characterized by its cytokine-secretion profile which is intimately associated to the effector functions. Th1 cells mediate cellular immunity against intracellular bacteria and viruses by secreting cytokines such as IFN-γ and tumour necrosis factor-α (TNF-α) Th2 cells regulate humoral immunity and immunity against extracellular parasites by producing IL-4, IL-5 and IL-13.

1. Burnet FM. The Clonal Selection Theory of Acquired Immunity. Nashville, TN:Vanderbilt University Press, 1959.

2. Zinkernagel RM. Restriction by H-2 gene complex of transfer of cell-mediated immunity to Listeria monocytogenes. Nature 1974; 251:230.

3. Cunningham AJ, Lafferty KJ. A simple conservative explanation of the H-2 restriction of interactions between lymphocytes. Scand J Immunol 1977;6:1.

4. Linsley PS, Clark EA, Ledbetter JA. T-cell antigen CD28 mediates adhesion with B cells by interacting with activation antigen B7/BB-1. Proc Natl Acad Sci U S A 1990;87:5031.

7. Scott P. IL-12: initiation cytokine for cell-mediated immunity. Science 1993;260:496.

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